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Çѱ¹½Ä¹°ÇÐȸ / v.24, no.4, 1981³â, pp.171-179
¿Á¼ö¼ö »Ñ¸®·ÎºÎÅÍ ºÐ¸®ÇÑ Membrane-bound ATPaseÀÇ Æ¯¼º¿¡ °üÇÑ ¿¬±¸
( Characterization of the Membrane-bound Adenosine Triphosphatase from Corn Roots )
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¿Á¼ö¼ö »Ñ¸®·ÎºÎÅÍ ºÐ¸®ÇÑ 13,000g pellet°ú 13,000~80,000g pellet ³»¿¡ ÀÖ´Â membrane-bound ATPasesÀÇ Æ¯¼ºÀ» ±¸¸íÇÏ¿´´Ù. 13,000g pellet°ú 13,000~80,000g pelletÀÇ membrane-bound ATPasesÀÇ ÃÖÀû pH´Â 5¿Í 9¿´´Ù. Discontinuous sucrose gradient centrifugation¿¡ ÀÇÇÑ 13,000g pelletÀÇ ºÐȹÁß Fraction C´Â pH 5¿¡¼­, Fraction D, E ¹× F´Â pH 5¿¡¼­º¸´Ù pH 9¿¡¼­ ´õ³ôÀº Ȱ¼ºÀ» ³ªÅ¸³Â´Ù. 13,000~80,000g pelletÀÇ ºÐȹ¿¡¼­ º¸¸é, Fraction A, C´Â pH 9º¸´Ù pH 5¿¡¼­, Fraction B, D, E ¹× F´Â pH 5º¸´Ù pH 9¿¡¼­ ´õ ³ôÀº Ȱ¼ºÀ» °¡°Ú´Ù. pH 5¿Í pH 9¿¡¼­ membrane-bound ATPasesÀÇ ±âÁúÆ÷È­ ³óµµ´Â 3~5 mMÀ̸ç ATP¿¡ ´ëÇÑ Km °ªÀº ¸ðµÎ 0.25 mMÀÌ¿´´Ù. Vmax °ªÀº 8.0~55.6 $mu$M Pi/mg membrane protein/hrÀÇ ¹üÀ§¿¡ ÀÖ¾ú´Ù. Membrane-bound ATPaseÀÇ È°¼ºÀº $K^+$ À̿¿¡ ÀÇÇØ Áõ°¡µÇ¾ú´Ù.
The membrane-bound ATPases were separated on sucrose gradient from corn roots and characterized by pH optima, sensitivity to monovalent salt, Km and Vmax. The pH optima for the activity of all the ATPases associated with 13, 000g pellet and 13, 000~80, 000g pellet were 5 and 9, respectively. The ATPases in Fractions B and C of the 13, 000 g pellet were more active at pH 5 than pH 9. While, in the case of Fractions D, E and F, they were reverse. The activities of the ATPase in Fractions A and C of the 13, 000~80, 000 g pellet were greater at pH 5 than pH 9. On the other hand, the ATPases in Fractions B, D, E, and F were more active at pH 9 than pH 5. The optimum concentraction of ATP for the assay was about 3 to 5 mM. The Km's for the membrane-bound ATPases in 13, 000g pellet and in 13, 000~80, 000 g pellet were 0.25 mM. While Vmax values for 13, 000g pellet were from 8.0 to 12.5 $mu$M Pi/mg protein/hr. according to pH values, those for 13, 000~80, 000 g pellet were from 35.7 to 55.6 $mu$M Pi/mg protein/hr. Activities of the membrane-bound ATPases in both 13, 000 g pellet and 13, 000~80, 000 g pellet were stimulated with increasing the concentration of $K^+$.
 
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Journal of Plant Biology / v.24, no.4, 1981³â, pp.171-179
Çѱ¹½Ä¹°ÇÐȸ
ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO198111922411174)
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³í¹® Á¦°ø : KISTI Çѱ¹°úÇбâ¼úÁ¤º¸¿¬±¸¿ø
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